Abstract

AbstractThe effect of cooking on proteins from acha and durum wheat was assessed from an analysis of protein extractability, gel electrophoretic profiles, in‐vitro protein digestibility (IVPD) and the amino acid compositions of wholemeal flour and residue proteins. Heating wholemeal flour samples at 100–140°C (t = 10–40 min) resulted in 0–30% and 45–55% decreases in acha and durum protein solubility, respectively. In general, high molecular weight (30–70 k Da) protein subunits were more susceptible to heat damage. For both cereals, sodium dodecyl sulphate (SDS; 10 g litre−1) and/or dithiothrcitol (DTT; 10 mM) increased protein solubility in unheated and heated samples. The IVPD index was 90–91% and was not significantly altered by cooking (100–120°C, t = 40 min). Cooking at extreme temperatures (140°C, t = 40 min) reduced the IVPD by 8% (P = 0.05). Osborne fractionation resulted in a durum or acha residue level of 7.8% or 55.2%. Treatment with solvent containing propanol, SDS and/or DTT at room temperature followed by SDS‐polyacrylamide gel electrophoresis of non‐solubilised proteins showed that the glutelin fraction of acha, with the exception of a 65 kDa subunit, was insoluble owing to strong inter‐subunit hydrophobic and disulphide interactions. Wholemeal acha flour and residue protein showed a significantly greater level of hydrophobic and sulphur amino acids as well as glutamine which is associated with H‐bonding. The possibility that cereal protein solubility is also dependent on protein‐carbohydrate links is discussed.

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